4pg6 | pdb_00004pg6

Crystal structure of S. aureus Homoserine Dehydrogenase at pH7.0

spinqualitylabelsall models 4pg6, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pg6 is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, DMS, GOL, PEG Related: 4pg4, 4pg5, 4pg7, 4pg8 Gene: hom, CH51_06975, JN533_07120, QT38_06630, SASCBU26_01217 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885) Activity: Homoserine dehydrogenase, with EC number 1.1.1.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. This enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. Here, a structural rationale for the hydride-transfer step in the reaction mechanism of HSD is reported. The structure of Staphylococcus aureus HSD was determined at different pH conditions to understand the basis for the enhanced enzymatic activity at basic pH. An analysis of the crystal structure revealed that Lys105, which is located at the interface of the catalytic and cofactor-binding sites, could mediate the hydride-transfer step of the reaction mechanism. The role of Lys105 was subsequently confirmed by mutational analysis. Put together, these studies reveal the role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Structural basis for the catalytic mechanism of homoserine dehydrogenase.,Navratna V, Reddy G, Gopal B Acta Crystallogr D Biol Crystallogr. 2015 May;71(Pt 5):1216-25. doi:, 10.1107/S1399004715004617. Epub 2015 Apr 30. PMID:25945586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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